2. What does the Bohr effect mean? a) describe this phenomenon: b) represent the graph which shows the oxygen -binding affinity of hemoglobin in resting and contracting muscle capillaries; c) explain the difference of the curves: d) give another examples of situations in which hemoglobin oxygen-binding affinity can be changed; explain the biological significance of these changing.

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2. What does the Bohr effect mean? a) describe this phenomenon: b) represent the graph which shows the oxygen -binding affinity of hemoglobin in resting and contracting muscle capillaries; c) explain the difference of the curves: d) give another examples of situations in which hemoglobin oxygen-binding affinity can be changed; explain the biological significance of these changing.

Answer 1

a) The Bohr effect refers to the phenomenon where the oxygen-binding affinity of hemoglobin decreases as the concentration of carbon dioxide (CO2) and hydrogen ions (H+) increases. This effect is named after the Danish physiologist Christian Bohr, who first described it in 1904.b) The graph representing the oxygen-binding affinity of hemoglobin in resting and contracting muscle capillaries would show two curves. The curve for resting muscle capillaries would be higher, indicating a higher oxygen-binding affinity, while the curve for contracting muscle capillaries would be lower, indicating a lower oxygen-binding affinity.c) The difference in the curves represents the Bohr effect. In resting muscle capillaries, the oxygen-binding affinity of hemoglobin is higher, meaning that hemoglobin has a greater tendency to bind to oxygen. However, in contracting muscle capillaries, the oxygen-binding affinity of hemoglobin is lower, meaning that hemoglobin has a lesser tendency to bind to oxygen. This is because the increased CO2 and H+ concentration in contracting muscles reduces the affinity of hemoglobin for oxygen, allowing more oxygen to be released to the tissues that need it.d) Other examples of situations in which hemoglobin oxygen-binding affinity can be changed include:1. Increased temperature: As the temperature increases, the oxygen-binding affinity of hemoglobin decreases. This is because the increased kinetic energy of the molecules causes the hemoglobin to release more oxygen.2. Increased levels of 2,3-bisphosphoglycerate (2,3-BPG): 2,3-BPG is a byproduct of red blood cell metabolism and can bind to hemoglobin, reducing its oxygen-binding affinity. This is particularly important in tissues with high metabolic rates, such as muscles, where more oxygen is needed.3. Increased levels of carbon monoxide (CO): Carbon monoxide can bind to hemoglobin with high affinity, reducing its oxygen-binding affinity. This can be harmful, as it can lead to tissue hypoxia and carbon monoxide poisoning.The biological significance of these changes in hemoglobin oxygen-binding affinity is that they allow the body to regulate oxygen delivery to tissues based on their metabolic needs. For example, in contracting muscles, the Bohr effect and other factors can reduce the oxygen-binding affinity of hemoglobin, allowing more oxygen to be released to the tissues that need it. This helps to meet the increased oxygen demand during muscle contraction.

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